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TitleIntroduction and characterization of a functionally linked metal ion binding site at the exposed heme edge of myoglobin
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 100, Page 3647-3652, Year 2003
Publish dateFeb 15, 2003 (structure data deposition date)
AuthorsHunter, C.L. / Maurus, R. / Mauk, M.R. / Lee, H. / Raven, E.L. / Tong, H. / Nguyen, N. / Smith, M. / Brayer, G.D. / Mauk, A.G.
External linksProc. Natl. Acad. Sci. USA / PubMed:12644706
MethodsX-ray diffraction
Resolution1.6 - 1.9 Å
Structure data

PDB-1nz2:
K45E Variant of Horse Heart Myoglobin
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1nz3:
K45E-K63E Variant of Horse Heart Myoglobin
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-1nz4:
The horse heart myoglobin variant K45E/K63E complexed with Cadmium
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1nz5:
The Horse heart myoglobin variant K45E/K63E complexed with Manganese
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-HOH:
WATER

ChemComp-CD:
Unknown entry

ChemComp-MN:
Unknown entry

Source
  • equus caballus (horse)
KeywordsOXYGEN STORAGE/TRANSPORT / muscle / oxygen transport / heme / OXYGEN STORAGE-TRANSPORT COMPLEX / Horse heart myoglobin / cadmium Cd2+ horse heart myoglobin engineered metal binding site / Manganese Mn2+ horse heart myoglobin engineered metal binding site

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